oligosaccharide/sarcoma

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Transformation-dependent alterations in the oligosaccharides of Prague C Rous sarcoma virus glycoproteins.

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The influence of cell transformation on the glycosylation of viral envelope glycoproteins was examined by high-resolution gel filtration and specific glycosidase digestions of 3H-sugar-labeled glycopeptides from nondefective and transformation-defective Prague C strains of Rous sarcoma virus

Rous sarcoma virus glycoproteins contain hybrid-type oligosaccharides.

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Examination of [3H]mannose-labeled glycopeptides from Prague C Rous sarcoma virus gp85 with gel filtration and sequential glycosidase digestions demonstrated the presence of hybrid-type asparaginyl-oligosaccharides. The major hybrid species had an oligomannosyl core (Man5GlcNAc2-ASN) characteristic

Oligosaccharides of the Hazelhurst vesicular stomatitis virus glycoprotein are more extensively processed in Rous sarcoma virus-transformed baby hamster kidney cells.

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Because of the extensive oligosaccharide heterogeneity of the membrane glycoprotein (G) from the Hazelhurst strain of vesicular stomatitis virus, this virus has been used as a specific intracellular probe of altered protein glycosylation in Rous sarcoma virus-transformed versus normal baby hamster

Processing of gPr92env, the precursor to the glycoproteins of Rous sarcoma virus: use of inhibitors of oligosaccharide trimming and glycoprotein transport.

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A number of aspects of the processing of gPr92env, the precursor to the viral glycoproteins gp85 and gp35 of Rous sarcoma virus (RSV), have been studied. First, the kinetics of gPr92env processing have been examined, revealing that the precursor is overproduced in the infected cell and only a small

Both acidic-type and neutral-type asparaginyl-oligosaccharides of host-cell glycoproteins are altered in Rous-sarcoma-virus-transformed chick-embryo fibroblasts.

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In comparisons of [3H]mannose-labelled glycopeptides from chick-embryo fibroblasts infected and transformed with non-defective Prague C Rous-sarcoma virus and from untransformed fibroblasts infected with a transformation-defective derivative of Prague C Rous-sarcoma virus, we have detected

Lectin affinity chromatography of Sindbis and Rous sarcoma virus glycopeptides and oligosaccharides.

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Glycopeptides and endogly cosidase-digested oligosaccharides from [3H]mannose-labeled Rous sarcoma virus and Sinbis virus have been fractionated by lentil lectin-Sepharose and concanavalin A-agarose affinity chromatography and subsequently analyzed by BioGel P-4 gel filtration. Only a specific

Oligosaccharide modifications and the site of processing of gPr92env, the precursor for the viral glycoproteins of Rous sarcoma virus.

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D-galactosyltransferase and its endogenous substrates in chick embryo fibroblasts transformed by Rous sarcoma virus.

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UDP-D-galactose: 2-acetamido-2-deoxy-beta-D-glucopyranosyl 4-beta-D-galactosyltransferase (GalTase) activity was purified, from primary chick embryo fibroblast (CEF) transformed by a temperature-sensitive, Rous sarcoma virus mutant (CEF-RSV), by chromatography on an affinity resin prepared with

Oligosaccharide chains of avian RNA tumor virus glycoproteins contain heterogeneous oligomannosyl cores.

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Chicken embryo fibroblasts (C/E phenotype) infected with subgroups B and C of the Prague strain of Rous sarcoma virus were radiolabeled with either [6-(3)H]-glucosamine or [2-(3)H]mannose, and virus was purified from the growth medium. The large envelope glycoprotein, gp85, was the only major

Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels.

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The major excreted protein of transformed mouse fibroblasts (MEP) has recently been identified as the lysosomal cysteine protease, cathepsin L. The synthesis and intracellular trafficking of this protein in mouse fibroblasts are regulated by growth factors and malignant transformation. To further

Inhibition of mannose incorporation into glycoproteins and dolichol-linked intermediates of Sarcoma 180 cells by 6-methylmercaptopurine ribonucleoside.

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6-Methylmercaptopurine ribonucleoside (6-MMPR), an inhibitor of purine nucleotide biosynthesis de novo, was used as a model compound to evaluate the relationship between the levels of intracellular guanosine triphosphate (GTP) and the formation of cellular glycoproteins and their

Growth-inhibition of S180 residual-tumor by combination of cyclophosphamide and chitosan oligosaccharides in vivo.

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Chitosan oligosaccharides (COS), hydrolyzed products of chitosan, have recently been reported to have various biological activities. Herein, the present study was undertaken to assess the ability of COS to potentiate the antitumor effect of cyclophosphamide (CTX) as well as alleviating the

Replica exchange molecular dynamics simulations reveal the structural and molecular properties of levan-type fructo-oligosaccharides of various chain lengths.

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BACKGROUND Levan and levan-type fructo-oligosaccharides (LFOs) have various potential applications in pharmaceutical and food industries due to their beneficial properties such as their low intrinsic viscosity and high water solubility. Previous studies showed that they exhibited prebiotic effects,

Characterization of viral polyproteins in cells transformed and producing Moloney murine sarcoma virus-124.

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The viral proteins of Moloney murine sarcoma virus-transformed mouse cells (G8-124), that overproduce the sarcoma virus relative to helper leukemia virus, were examined by immunoprecipitation, sizing by gel electrophoresis and peptide mapping. Using antisera to the viral core proteins, a

THE ISOLATION AND PARTIAL CHARACTERIZATION OF THE GLYCOLIPIDS OF BP8/C3H ASCITES-SARCOMA CELLS.

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1. The total lipid was extracted from BP8/C3H ascites-sarcoma cells with acetone, light petroleum, pyridine and chloroform-methanol successively. Each extract was treated with mild alkali. The alkali-stable lipids from the pyridine and chloroform-methanol extracts, which included the glycolipids,

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